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Volumn 52, Issue 5, 2004, Pages 1293-1299

Modification of Ovalbumin with a Rare Ketohexose through the Maillard Reaction: Effect on Protein Structure and Gel Properties

Author keywords

D psicose; Gelling property; Glycation; Maillard reaction; Ovalbumin

Indexed keywords

FRUCTOSE; GELLING AGENT; GLUCOSE; KETOSE; OVALBUMIN; TRYPTOPHAN;

EID: 1542376970     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf030428s     Document Type: Article
Times cited : (163)

References (37)
  • 1
    • 0032825597 scopus 로고    scopus 로고
    • Improvement of functional properties of ovalbumin by conjugation with glucuronic acid through the Maillard reaction
    • Aoki, T.; Hiidome, Y.; Kitahata, K.; Sugimoto, Y.; Ibrahim, H. R.; Kimura, T.; Kato, Y. Improvement of functional properties of ovalbumin by conjugation with glucuronic acid through the Maillard reaction. Food Res. Int. 1999, 32, 129-133.
    • (1999) Food Res. Int. , vol.32 , pp. 129-133
    • Aoki, T.1    Hiidome, Y.2    Kitahata, K.3    Sugimoto, Y.4    Ibrahim, H.R.5    Kimura, T.6    Kato, Y.7
  • 2
    • 0031177718 scopus 로고    scopus 로고
    • Improvement of functional properties of β-lactoglobulin by conjugation with glucose-6-phosphate through the Maillard reaction
    • Aoki, T.; Kitahata, K.; Fukumoto, T.; Sugimoto, Y.; Ibrahim, H. R.; Kimura, T.; Kato, Y.; Matsuda, T. Improvement of functional properties of β-lactoglobulin by conjugation with glucose-6-phosphate through the Maillard reaction. Food Res. Int. 1997, 30, 401-406.
    • (1997) Food Res. Int. , vol.30 , pp. 401-406
    • Aoki, T.1    Kitahata, K.2    Fukumoto, T.3    Sugimoto, Y.4    Ibrahim, H.R.5    Kimura, T.6    Kato, Y.7    Matsuda, T.8
  • 3
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation
    • Morgan, F.; Léonil, J.; Mollé, D.; Bouhallab, S. Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation. J. Agric. Food Chem. 1999, 47, 83-91.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 83-91
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 4
    • 0000498147 scopus 로고
    • Improvement of emulsifying properties of egg white proteins by the attachment of polysaccharide through Maillard reaction in a dry state
    • Kato, A.; Minaki, K.; Kobayashi, K. Improvement of emulsifying properties of egg white proteins by the attachment of polysaccharide through Maillard reaction in a dry state. J. Agric. Food Chem. 1993, 41, 540-543.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 540-543
    • Kato, A.1    Minaki, K.2    Kobayashi, K.3
  • 5
    • 0000409683 scopus 로고
    • Preparation and characterization of ovalbumin-dextran conjugate having excellent emulsifying properties
    • Kato, A.; Murata, K.; Kobayashi, K. Preparation and characterization of ovalbumin-dextran conjugate having excellent emulsifying properties. J. Agric. Food Chem. 1988, 36, 421-425.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 421-425
    • Kato, A.1    Murata, K.2    Kobayashi, K.3
  • 6
    • 0001643044 scopus 로고
    • Modification of ovalbumin with glucose 6-phosphate by aminocarbonyl reaction. Improvement of protein heat stability and emulsifying
    • Kato, Y.; Aoki, T.; Kato, N.; Nakamura, N.; Matsuda, T. Modification of ovalbumin with glucose 6-phosphate by aminocarbonyl reaction. Improvement of protein heat stability and emulsifying. J. Agric. Food Chem. 1995, 43, 301-305.
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 301-305
    • Kato, Y.1    Aoki, T.2    Kato, N.3    Nakamura, N.4    Matsuda, T.5
  • 7
    • 0000668338 scopus 로고
    • Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides
    • Nakamura, S.; Kato, A.; Kobayashi, K. Enhanced antioxidative effect of ovalbumin due to covalent binding of polysaccharides. J. Agric. Food Chem. 1992, 40, 2033-2037.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 2033-2037
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 8
    • 21344456480 scopus 로고    scopus 로고
    • Bovin serum albumin gelation as a result of the Maillard reaction
    • Mat Easa, A.; Hill, S. E.; Mitchell, J. R.; Taylor, A. J. Bovin serum albumin gelation as a result of the Maillard reaction. Food Hydrocolloids 1996, 10, 199-202.
    • (1996) Food Hydrocolloids , vol.10 , pp. 199-202
    • Mat Easa, A.1    Hill, S.E.2    Mitchell, J.R.3    Taylor, A.J.4
  • 9
    • 0037014322 scopus 로고    scopus 로고
    • Improvement of gel properties of dried egg white by modification with galactomannan through the Maillard reaction
    • Matsudomi, N.; Nakano, K.; Soma, A.; Ochi, A. Improvement of gel properties of dried egg white by modification with galactomannan through the Maillard reaction. J. Agric. Food Chem. 2002, 50, 4113-4118.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4113-4118
    • Matsudomi, N.1    Nakano, K.2    Soma, A.3    Ochi, A.4
  • 10
    • 0032822981 scopus 로고    scopus 로고
    • Functional improvement in dried egg white through the Maillard reaction
    • Handa, A.; Kuroda, N. Functional improvement in dried egg white through the Maillard reaction. J. Agric. Food Chem. 1999, 47, 1845-1850.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 1845-1850
    • Handa, A.1    Kuroda, N.2
  • 11
    • 0037070365 scopus 로고    scopus 로고
    • Heat-induced gels of egg white/ovalbumin from five avian species: Thermal aggregation, molecular forces involved, and rheological properties
    • Sun, Y.; Hayakawa, S. Heat-induced gels of egg white/ovalbumin from five avian species: Thermal aggregation, molecular forces involved, and rheological properties. J. Agric. Food Chem. 2002, 50, 1636-1642.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 1636-1642
    • Sun, Y.1    Hayakawa, S.2
  • 12
    • 0036202220 scopus 로고    scopus 로고
    • Bioproduction strategies for rare hexose sugars
    • Izumori, K. Bioproduction strategies for rare hexose sugars. Naturwissenschaften 2002, 89, 120-124.
    • (2002) Naturwissenschaften , vol.89 , pp. 120-124
    • Izumori, K.1
  • 13
    • 0035536718 scopus 로고    scopus 로고
    • Dietary D-psicose, a C-3 epimer of D-fructose, suppresses the activity of hepatic lipogenic enzymes in rats
    • Matuso, T.; Baba, Y.; Hashiguchi, M.; Takeshita, K.; Izumori, K.; Suzuki, H. Dietary D-psicose, a C-3 epimer of D-fructose, suppresses the activity of hepatic lipogenic enzymes in rats. Asia Pacific J. Clin. Nutr. 2001, 10, 233-237.
    • (2001) Asia Pacific J. Clin. Nutr. , vol.10 , pp. 233-237
    • Matuso, T.1    Baba, Y.2    Hashiguchi, M.3    Takeshita, K.4    Izumori, K.5    Suzuki, H.6
  • 14
    • 0034551786 scopus 로고    scopus 로고
    • Rare sugars and sugar-based synthons by chemo-enzymatic synthesis
    • Giffhorn, F.; Köpper, S.; Huwig, A.; Freimund, S. Rare sugars and sugar-based synthons by chemo-enzymatic synthesis. Enzyme Microb. Technol. 2000, 27, 734-742.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 734-742
    • Giffhorn, F.1    Köpper, S.2    Huwig, A.3    Freimund, S.4
  • 15
    • 0035038912 scopus 로고    scopus 로고
    • Biotransformation of D-galactitol to tagatose by acetic acid bacteria
    • Manzoni, M.; Rollini, M. Bergomi, S. Biotransformation of D-galactitol to tagatose by acetic acid bacteria. Process Biochem. 2001, 36, 971-977.
    • (2001) Process Biochem. , vol.36 , pp. 971-977
    • Manzoni, M.1    Rollini, M.2    Bergomi, S.3
  • 16
    • 0034302040 scopus 로고    scopus 로고
    • Mass production of D-psicose from D-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase
    • Takeshita, K.; Suga, A.; Takada, G.; Izumori, K. Mass production of D-psicose from D-fructose by a continuous bioreactor system using immobilized D-tagatose 3-epimerase. J. Biosci. Bioeng. 2000, 90, 453-455.
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 453-455
    • Takeshita, K.1    Suga, A.2    Takada, G.3    Izumori, K.4
  • 18
    • 0034849389 scopus 로고    scopus 로고
    • Thermally induced aggregates in mixture of α-lactalbumin with ovalbumins from different avian species
    • Sun, Y.; Hayakawa, S. Thermally induced aggregates in mixture of α-lactalbumin with ovalbumins from different avian species. J. Agric. Food Chem. 2001, 49, 2511-2517.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2511-2517
    • Sun, Y.1    Hayakawa, S.2
  • 19
    • 0014052385 scopus 로고
    • Modification of amino groups in inhibitors of proteolytic enzymes
    • Haynes, R.; Osuga, D. T.; Feeney, R. E. Modification of amino groups in inhibitors of proteolytic enzymes. Biochemistry 1967, 6, 541-547.
    • (1967) Biochemistry , vol.6 , pp. 541-547
    • Haynes, R.1    Osuga, D.T.2    Feeney, R.E.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
  • 23
    • 0001221912 scopus 로고
    • Contribution of the hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin
    • Hayakawa, S.; Nakai, S. Contribution of the hydrophobicity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 1985, 18, 290-295.
    • (1985) Can. Inst. Food Sci. Technol. J. , vol.18 , pp. 290-295
    • Hayakawa, S.1    Nakai, S.2
  • 24
    • 0036284961 scopus 로고    scopus 로고
    • Chemical and biochemical properties of casein-sugar Maillard reaction products
    • Jing, H.; Kitts, D. D. Chemical and biochemical properties of casein-sugar Maillard reaction products. Food Chem. Toxicol. 2002, 40, 1007-1015.
    • (2002) Food Chem. Toxicol. , vol.40 , pp. 1007-1015
    • Jing, H.1    Kitts, D.D.2
  • 25
    • 0001039109 scopus 로고    scopus 로고
    • Reaction conditions influence the elementary composition and metal chelating affinity of nondialyzable model Maillard reaction products
    • Wijewickreme, A. N.; Kitts, D. D.; Durance, T. D. Reaction conditions influence the elementary composition and metal chelating affinity of nondialyzable model Maillard reaction products. J. Agric. Food Chem. 1997, 45, 4577-4583.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4577-4583
    • Wijewickreme, A.N.1    Kitts, D.D.2    Durance, T.D.3
  • 26
    • 0041662034 scopus 로고
    • Paramagnetic behaviour of model system melanoidins
    • Wu, C. H.; Russell, G.; Powrie, W. D. Paramagnetic behaviour of model system melanoidins. J. Food Sci. 1987, 52, 813-816, 822.
    • (1987) J. Food Sci. , vol.52 , pp. 813-816
    • Wu, C.H.1    Russell, G.2    Powrie, W.D.3
  • 27
    • 0001039110 scopus 로고    scopus 로고
    • Influence of reaction conditions on the oxidative behavior of model Maillard reaction products
    • Wijewickreme, A. N.; Kitts, D. D. Influence of reaction conditions on the oxidative behavior of model Maillard reaction products. J. Agric. Food Chem. 1997, 45, 4571-4576.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4571-4576
    • Wijewickreme, A.N.1    Kitts, D.D.2
  • 28
    • 0032864734 scopus 로고    scopus 로고
    • Reactivities of D-glucose and D-fructose during glycation of bovine serum albumin
    • Yeboah, F. K.; Alli, I.; Yaylayan, V. A. Reactivities of D-glucose and D-fructose during glycation of bovine serum albumin. J. Agric. Food Chem. 1999, 47, 3164-3172.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 3164-3172
    • Yeboah, F.K.1    Alli, I.2    Yaylayan, V.A.3
  • 29
    • 84985269010 scopus 로고
    • Maillard browning of common amino acids and sugars
    • Ashoor, S. H.; Zent, J. B. Maillard browning of common amino acids and sugars. J. Food Sci. 1984, 49, 1206-1207.
    • (1984) J. Food Sci. , vol.49 , pp. 1206-1207
    • Ashoor, S.H.1    Zent, J.B.2
  • 30
    • 0033916712 scopus 로고    scopus 로고
    • Mutagenicity of heated sugar-casein systems: Effect of the Maillard reaction
    • Brands, C. M. J.; Alink, G. M.; Boekel, M. J. S.; Jongen, W. M. F. Mutagenicity of heated sugar-casein systems: effect of the Maillard reaction. J. Agric. Food Chem. 2000, 48, 2271-2275.
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 2271-2275
    • Brands, C.M.J.1    Alink, G.M.2    Boekel, M.J.S.3    Jongen, W.M.F.4
  • 31
    • 0027317391 scopus 로고
    • Nonenzymatic glycation alters protein structure and stability: A study of two eye lens crystallins
    • Luthra, M.; Balasubramanian, D. Nonenzymatic glycation alters protein structure and stability: A study of two eye lens crystallins. J. Biol. Chem. 1993, 268, 18119-18127.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18119-18127
    • Luthra, M.1    Balasubramanian, D.2
  • 32
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct., Funct. Genet. 1989, 6, 87-103.
    • (1989) Proteins: Struct., Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 33
    • 0027543524 scopus 로고
    • Molten globule state of food proteins
    • Hirose, M. Molten globule state of food proteins. Trends Food Sci. Technol. 1993, 4, 48-51.
    • (1993) Trends Food Sci. Technol. , vol.4 , pp. 48-51
    • Hirose, M.1
  • 34
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end-products: A review
    • Singh, R.; Barden, A.; Mori, T.; Beilin, L. Advanced glycation end-products: a review. Diabetologia 2001, 44, 129-146.
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 35
    • 0022931516 scopus 로고
    • ε-carboxymethyllysine as a degradation product of fructose-lysine in glycated protein
    • ε-carboxymethyllysine as a degradation product of fructose-lysine in glycated protein. J. Biol. Chem. 1986, 261, 4889-4894.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 36
    • 0028951461 scopus 로고
    • Mechanism of autoxidative glycosylaton: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose
    • Wells-Knecht, K. J.; Zyzak, D. V.; Litchfield, J. E.; Thorpe, S. R.; Baynes, J. W. Mechanism of autoxidative glycosylaton: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry 1995, 34, 3702-3709.
    • (1995) Biochemistry , vol.34 , pp. 3702-3709
    • Wells-Knecht, K.J.1    Zyzak, D.V.2    Litchfield, J.E.3    Thorpe, S.R.4    Baynes, J.W.5
  • 37
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates in the Maillard reaction
    • Glomb, M.; Monnier, V. M. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates in the Maillard reaction. J. Biol. Chem. 1995, 270, 10017-10026.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10017-10026
    • Glomb, M.1    Monnier, V.M.2


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